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Q88AB2 (MASZ1_PSESM) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 81. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Malate synthase G 1

EC=2.3.3.9
Gene names
Name:glcB1
Synonyms:glcB-1
Ordered Locus Names:PSPTO_0480
OrganismPseudomonas syringae pv. tomato (strain DC3000) [Complete proteome] [HAMAP]
Taxonomic identifier223283 [NCBI]
Taxonomic lineageBacteriaProteobacteriaGammaproteobacteriaPseudomonadalesPseudomonadaceaePseudomonas

Protein attributes

Sequence length725 AA.
Sequence statusComplete.
Protein existenceInferred from homology

General annotation (Comments)

Function

Involved in the glycolate utilization. Catalyzes the condensation and subsequent hydrolysis of acetyl-coenzyme A (acetyl-CoA) and glyoxylate to form malate and CoA By similarity. HAMAP-Rule MF_00641

Catalytic activity

Acetyl-CoA + H2O + glyoxylate = (S)-malate + CoA. HAMAP-Rule MF_00641

Cofactor

Magnesium By similarity. HAMAP-Rule MF_00641

Pathway

Carbohydrate metabolism; glyoxylate cycle; (S)-malate from isocitrate: step 2/2. HAMAP-Rule MF_00641

Subunit structure

Monomer By similarity. HAMAP-Rule MF_00641

Subcellular location

Cytoplasm By similarity HAMAP-Rule MF_00641.

Sequence similarities

Belongs to the malate synthase family. GlcB subfamily.

Ontologies

Keywords
   Biological processGlyoxylate bypass
Tricarboxylic acid cycle
   Cellular componentCytoplasm
   LigandMagnesium
Metal-binding
   Molecular functionTransferase
   PTMOxidation
   Technical termComplete proteome
Gene Ontology (GO)
   Biological_processglyoxylate cycle

Inferred from electronic annotation. Source: UniProtKB-HAMAP

tricarboxylic acid cycle

Inferred from electronic annotation. Source: UniProtKB-KW

   Cellular_componentcytoplasm

Inferred from electronic annotation. Source: UniProtKB-SubCell

   Molecular_functionmalate synthase activity

Inferred from electronic annotation. Source: UniProtKB-HAMAP

metal ion binding

Inferred from electronic annotation. Source: UniProtKB-KW

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 725725Malate synthase G 1 HAMAP-Rule MF_00641
PRO_0000166894

Regions

Region125 – 1262Acetyl-CoA binding By similarity
Region457 – 4604Glyoxylate binding By similarity

Sites

Active site3401Proton acceptor By similarity
Active site6311Proton donor By similarity
Metal binding4321Magnesium By similarity
Metal binding4601Magnesium By similarity
Binding site1181Acetyl-CoA; via carbonyl oxygen By similarity
Binding site2761Acetyl-CoA By similarity
Binding site3131Acetyl-CoA By similarity
Binding site3401Glyoxylate By similarity
Binding site4321Glyoxylate By similarity
Binding site5411Acetyl-CoA; via carbonyl oxygen By similarity

Amino acid modifications

Modified residue6171Cysteine sulfenic acid (-SOH) By similarity

Sequences

Sequence LengthMass (Da)Tools
Q88AB2 [UniParc].

Last modified April 30, 2003. Version 1.
Checksum: F1993264E8083660

FASTA72579,144
        10         20         30         40         50         60 
MTEYVQVGDL QVARVLFDFV QNEATPGTGV DAGAFWAGAD QLIHDLAPKN KALLAQRDEL 

        70         80         90        100        110        120 
QAQIDAWHQS RAGQAHDASA YKAFLQEIGY LLPEAADFQI TTQNVDEEIA TMAGPQLVVP 

       130        140        150        160        170        180 
VMNARFALNA SNARWGSLYD ALYGTDAISE EGGAEKGKGY NKVRGDKVIA FARAFLDQAA 

       190        200        210        220        230        240 
PLAAGSHVDS TAYKLIDGRL VISLKGGSNT GLRDDAQLVG FQGDASAPFA VLFKHNGLHF 

       250        260        270        280        290        300 
ELQIDAASPV GQTDPAGVKD IVMEAALTTI MDCEDSIAAV DADDKVVVYR NWLGLMKGDL 

       310        320        330        340        350        360 
VESVSKGGET FTRTMNPDRV YTTPQGGEVT LHGRSLLFIR NVGHLMTIDA ILDKHGNEVP 

       370        380        390        400        410        420 
EGILDGLLTS LAAIHNLNGN NTRSNSRSGS MYIVKPKMHG PQEAAFTNEL FGRIEQVLGL 

       430        440        450        460        470        480 
PRNTLKVGIM DEERRTTVNL KACIQAASER VVFINTGFLD RTGDEIHTSM EAGPVVRKAQ 

       490        500        510        520        530        540 
MKAEKWISAY ENSNVDIGLK CGLQGRAQIG KGMWAMPDLM AAMLEQKIAH PLAGANTAWV 

       550        560        570        580        590        600 
PSPTAAALHA LHYHKVDVFA RQAELAQREQ ASVDDILTIP LALNTDWTPE QVQNELDNNA 

       610        620        630        640        650        660 
QGILGYVVRW IDQGVGCSKV PDINDIGLME DRATLRISSQ HMTNWLRHGI VTETQVLESL 

       670        680        690        700        710        720 
KRMAPVVDRQ NANDPLYRPL SPDFDSNIAF QAAVELVIEG TRQPNGYTEP VLHRRRREFK 


AKNRV 

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Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AE016853 Genomic DNA. Translation: AAO54024.1.
RefSeqNP_790329.1. NC_004578.1.

3D structure databases

ProteinModelPortalQ88AB2.
SMRQ88AB2. Positions 2-722.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING223283.PSPTO_0480.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaAAO54024; AAO54024; PSPTO_0480.
GeneID1182089.
KEGGpst:PSPTO_0480.
PATRIC19992138. VBIPseSyr93040_0497.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG2225.
HOGENOMHOG000220740.
KOK01638.
OMASQFIENE.
OrthoDBEOG6HJ286.
PhylomeDBQ88AB2.

Enzyme and pathway databases

BioCycPSYR223283:GJIX-477-MONOMER.
UniPathwayUPA00703; UER00720.

Family and domain databases

Gene3D2.170.170.11. 2 hits.
HAMAPMF_00641. Malate_synth_G.
InterProIPR011076. Malate_synth-like.
IPR023310. Malate_synth_G_beta_sub_dom.
IPR001465. Malate_synthase.
IPR006253. Malate_synthG.
[Graphical view]
PfamPF01274. Malate_synthase. 1 hit.
[Graphical view]
SUPFAMSSF51645. SSF51645. 1 hit.
TIGRFAMsTIGR01345. malate_syn_G. 1 hit.
ProtoNetSearch...

Entry information

Entry nameMASZ1_PSESM
AccessionPrimary (citable) accession number: Q88AB2
Entry history
Integrated into UniProtKB/Swiss-Prot: April 30, 2003
Last sequence update: April 30, 2003
Last modified: July 9, 2014
This is version 81 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

PATHWAY comments

Index of metabolic and biosynthesis pathways